Stimuli-responsive command polymer surface for generation of protein gradients

Ionov, Leonid; Houbenov, Nikolay; Sidorenko, Alexander; Stamm, Manfred; Minko, Sergiy

doi:10.1116/1.3119722

Cited by 43 publications

(37 citation statements)

References 51 publications

(44 reference statements)

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“…BSA) are negatively charged, and therefore a positive charged surface such as PEI modified MNP would favour protein adsorption. However, in addition to the electrostatic interaction which causes adsorption of protein on oppositely charged surfaces [9] , proteins have amphiphilic character which will cause the adsorption of protein onto similar charged surfaces [10] , which explain the interaction between BSA and negatively charged PMAA-MNP surface. The slower rate of aggregation of bare MNP indicated the there is also an interaction between BSA and surface of bare MNP, although the aggregation of bare MNP could not be fully prevented.…”

Section: Resultsmentioning

confidence: 99%

Effects of surface functional groups on the aggregation stability of magnetite nanoparticles in biological media containing serum

Wiogo

Lim

Bulmuş

et al. 2011

2011 11th IEEE International Conference on Nanotechnology

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-Size stability of magnetite nanoparticles (MNP) with different surface functional groups in biological media was achieved by the addition of fetal bovine serum (FBS). The stability of the particles was attributed to the formation of protein coronas around the particles, which provides sufficient steric hindrance to prevent aggregation of the particles. The stability of different modified MNP were also studied in biological media containing bovine serum albumin (BSA) to further understand the stabilization mechanism. BSA was found to stabilize polyethyleneimine (PEI) modified MNP and polymethacrylic acid (PMAA) coated MNP, but not the bare MNP. These results indicate a difference in interactions between serum protein and the MNP that is govern by the type of functional groups on the MNP surface, with positively charged surface groups resulting higher protein adsorption and better stability.

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Section: Resultsmentioning

confidence: 99%

Effects of surface functional groups on the aggregation stability of magnetite nanoparticles in biological media containing serum

Wiogo

Lim

Bulmuş

et al. 2011

2011 11th IEEE International Conference on Nanotechnology

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“…After the binding to these scaffolds, the tethered proteins must preserve their biological functions [76,[96][97][98]. The versatile structure, chemistry as well as tunable mechanical properties [99] of polymer brushes make these scaffolds very attractive candidates to bind and immobilize proteins.…”

Section: Immobilization Of Proteinsmentioning

confidence: 99%

Polymer Brushes with Precise Architectures for Molecular Biorecognition

Pérez-Perrino

Molina

Navarro

2015

Design of Polymeric Platforms for Selective Biorecognition

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“…3.20). The possibility of tuning and switching adhesion between stimuli-responsive materials and proteins and cells has been explored for the control of cell and protein adhesion [127], as well as exposing and masking potential biointerfaces and manipulation of cellular signals, protein interactions, and growth factors [128]. Moreover, precise control of the permeation of chemicals, nanoparticles, and ions through nanoporous membranes and 3D scaffolds offers a unique opportunity for control of assembly and growth process [129][130][131][132].…”

Section: 'Shaky' Foundations Of Biological Materialsmentioning

confidence: 99%

The Challenges of Biological Materials

Cranford

Buehler

2012

Biomateriomics

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The challenges of biological materials and systems-the inherent complexity-is a result of the diversity of Nature itself. The evolution of structure in biological materials is guided by the ever-changing requirements of the external environment and have resulted in materials with desirable engineering properties, such as high strength, toughness, adaptability, flaw tolerance, self-healing, mutability and multifunctionality, all with a limited set of-and frequently inferiorbuilding materials. As a result of such constraints, Nature implements a flexible material composed of a limited set of molecular components: soft, deformable, highly convoluted proteins, composed of a minute set of amino acids. Providing a common base, protein form and function has evolved intimately, such that even the prediction of folded structure from a known peptide sequence is a technological challenge. Potential functionality is extended through the use of structural hierarchies-resulting in system robustness, efficiency, and design tolerance-while decreasing the efficacy of any single-scale analysis. At the microscale, the complexity manifests as functional, growing, adaptable materials-producing "shaky" platforms for tissue engineering and growth. While biological and chemical cues may change across scales, mechanical insights can provide a common basis regardless of scale or analytical progression.Look deep into Nature, and then you will understand everything better.Albert Einstein (1879Einstein ( -1955

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Stimuli-responsive command polymer surface for generation of protein gradients

Cited by 43 publications

References 51 publications

Effects of surface functional groups on the aggregation stability of magnetite nanoparticles in biological media containing serum

Effects of surface functional groups on the aggregation stability of magnetite nanoparticles in biological media containing serum

Polymer Brushes with Precise Architectures for Molecular Biorecognition

The Challenges of Biological Materials

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